SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 7-STRANDED BARREL THIS IS REPRESENTED BY A 8-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "BB" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 7-STRANDED BARREL THIS IS REPRESENTED BY A 8-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.
Mass: 18.015 Da / Num. of mol.: 290 / Source method: isolated from a natural source / Formula: H2O
Compound details
ENGINEERED RESIDUE IN CHAIN A, CYS 1133 TO ALA ENGINEERED RESIDUE IN CHAIN B, CYS 1133 TO ALA
Sequence details
GLY AND SER AT THE N-TERMINUS OF THE PROTEIN IS DERIVED FROM THE TAG. ALA AT POSITION 139 IS A CYS ...GLY AND SER AT THE N-TERMINUS OF THE PROTEIN IS DERIVED FROM THE TAG. ALA AT POSITION 139 IS A CYS IN GENBANK SEQUENCE. THIS HAS BEEN MUTATED INTENTIONALLY.
-
Experimental details
-
Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
-
Sample preparation
Crystal
Density Matthews: 2.2 Å3/Da / Density % sol: 44.45 % / Description: NONE
Crystal grow
pH: 7.5 Details: 0.2 M KSCN,0.1 M BIS-TRIS PROPANE PH 7.5, 20% W/V POLY-ETHYLENE GLYCOL (PEG) 3350
Resolution: 1.578→48.032 Å / SU ML: 0.18 / σ(F): 1.4 / Phase error: 23.7 / Stereochemistry target values: ML Details: RESIDUES 124-130 OF CHAIN A INCLUSIVE ARE DISORDERED IN THS STRUCTURE AS ARE RESIDUES 124-131 INCLUSIVE OF CHAIN B.
Rfactor
Num. reflection
% reflection
Rfree
0.2084
2266
5 %
Rwork
0.1836
-
-
obs
0.1849
44931
93.94 %
Solvent computation
Shrinkage radii: 0.83 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 38.321 Å2 / ksol: 0.322 e/Å3
Displacement parameters
Baniso -1
Baniso -2
Baniso -3
1-
-5.1405 Å2
0 Å2
0 Å2
2-
-
14.401 Å2
0 Å2
3-
-
-
-9.2605 Å2
Refinement step
Cycle: LAST / Resolution: 1.578→48.032 Å
Protein
Nucleic acid
Ligand
Solvent
Total
Num. atoms
2585
0
0
290
2875
Refine LS restraints
Refine-ID
Type
Dev ideal
Number
X-RAY DIFFRACTION
f_bond_d
0.006
2679
X-RAY DIFFRACTION
f_angle_d
0.98
3660
X-RAY DIFFRACTION
f_dihedral_angle_d
11.609
908
X-RAY DIFFRACTION
f_chiral_restr
0.066
425
X-RAY DIFFRACTION
f_plane_restr
0.004
464
LS refinement shell
Resolution (Å)
Rfactor Rfree
Num. reflection Rfree
Rfactor Rwork
Num. reflection Rwork
Refine-ID
% reflection obs (%)
1.5781-1.6148
0.3027
113
0.2655
1905
X-RAY DIFFRACTION
64
1.6148-1.6552
0.2868
133
0.2424
2262
X-RAY DIFFRACTION
76
1.6552-1.7
0.2823
124
0.2214
2577
X-RAY DIFFRACTION
86
1.7-1.75
0.2555
158
0.2117
2828
X-RAY DIFFRACTION
94
1.75-1.8065
0.2233
166
0.1987
2929
X-RAY DIFFRACTION
98
1.8065-1.8711
0.2593
130
0.1868
2971
X-RAY DIFFRACTION
99
1.8711-1.946
0.1889
173
0.1776
2944
X-RAY DIFFRACTION
99
1.946-2.0346
0.2063
144
0.1796
2996
X-RAY DIFFRACTION
99
2.0346-2.1418
0.2135
145
0.1774
2958
X-RAY DIFFRACTION
98
2.1418-2.276
0.2084
145
0.1846
3033
X-RAY DIFFRACTION
99
2.276-2.4517
0.2439
152
0.1837
2997
X-RAY DIFFRACTION
100
2.4517-2.6984
0.2261
160
0.1938
3068
X-RAY DIFFRACTION
100
2.6984-3.0889
0.2183
160
0.1938
2991
X-RAY DIFFRACTION
98
3.0889-3.8914
0.1929
177
0.1833
3042
X-RAY DIFFRACTION
99
3.8914-48.0547
0.1788
186
0.1637
3164
X-RAY DIFFRACTION
99
Refinement TLS params.
Method: refined / Origin x: -5.0045 Å / Origin y: -12.5719 Å / Origin z: 25.112 Å
11
12
13
21
22
23
31
32
33
T
0.1501 Å2
-0.0061 Å2
-0.0063 Å2
-
0.102 Å2
0.0029 Å2
-
-
0.1443 Å2
L
0.8493 °2
0.1592 °2
-0.4588 °2
-
0.2507 °2
-0.2146 °2
-
-
1.4414 °2
S
-0.0195 Å °
0.0148 Å °
-0.0149 Å °
-0.0591 Å °
0.0037 Å °
0.0043 Å °
-0.1075 Å °
0.03 Å °
0.0071 Å °
Refinement TLS group
Selection details: ALL
+
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